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Structure paper

TitleE3 Ligase Rad18 Promotes Monoubiquitination Rather Than Ubiquitin Chain Formation by E2 Enzyme Rad6.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 108, Page 5590-, Year 2011
Publish dateMar 2, 2011 (structure data deposition date)
AuthorsHibbert, R.G. / Huang, A. / Boelens, R. / Sixma, T.K.
External linksProc. Natl. Acad. Sci. USA / PubMed:21422291
MethodsX-ray diffraction
Resolution1.5 - 2 Å
Structure data

PDB-2yb6:
Native human Rad6
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-2ybf:
Complex of Rad18 (Rad6 binding domain) with Rad6b
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsLIGASE / TRANSLESION SYNTHESIS / UBIQUITIN CHAIN SYNTHESIS / E2 UBIQUITIN CONJUGATING ENZYME / E3 UBIQUITIN LIGASE / PCNA UBIQUITINATION

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